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Featuring:
Plus
quality reagents for:
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| Agarose bound* Ricinus Communis Agglutinin I (RCA I, RCA120)
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This lectin consists of two subunits of 60 kDa which can be
dissociated by reducing agents into closely related chains
between 27 kDa and 33 kDa. One of the chains appears to be
common to the “B” chain of another castor bean lectin, ricin,
while the other chain is unique to RCA I.
Agarose bound* Ricinus communis agglutinin I is prepared using our affinity-purified
lectins. Heat stable, cross-linked 4% agarose beads with
a molecular weight exclusion limit of about 2x107 daltons
are used as the solid-phase matrix to which the lectins are
covalently coupled. The attachment of the lectins to the beads
is carefully controlled to preserve lectin activity and minimize
conformational changes of the bound lectins that might result
in nonspecific ionic or hydrophobic interactions. The technique
we have developed to couple lectins to agarose beads inserts a
hydrophilic spacer arm between the lectin and the matrix.
This coupling method provides several advantages over the
traditional cyanogen bromide procedure:
Maximum carbohydrate binding activity of the coupled
lectins is retained
Linkage is stable over a range of pH values
Conjugated proteins are not leached off the beads by Tris or
other routinely used buffers
No residual charges are present after conjugation. This
minimizes non-specific binding to the matrix.
Our agarose bound lectins are supplied at a constant
concentration of lectin per ml of settled beads. The
concentration for each lectin is selected to achieve the highest
glycoconjugate binding capacity per mg of lectin present in
the beads. Each lot is tested for its binding capacity using
glycoproteins known to bind the lectin. This provides a
guideline for the user and assures the quality of our agarose
bound lectins.
Inhibiting/Eluting Sugar: 200 mM galactose or lactose
*4 mg lectin/ml gel
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